RT Journal Article
SR Electronic
T1 A Nuclear Magnetic Resonance Study of Hapten-Antibody Interaction
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 399
OP 400
VO 3
IS 4
A1 SEYMOUR JOFFE
YR 1967
UL http://molpharm.aspetjournals.org/content/3/4/399.abstract
AB In the presence of purified specific antigalactosyl antibody, the hapten p-nitrophenyl-β-D-galactoside showed changes in its nuclear magnetic resonance (NMR) spectrum for those protons attached to the aromatic ring. These changes were interpreted as line broadening and thus indicated the most energetic site of attachment of the hapten to the antibody. This work was supported by U.S.P.H.S. Research Grants Nos. NB 03356-04 and NB 5114-08.